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Published on July 7, 2006; 10.1104/pp.106.081489


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Received April 4, 2006
Accepted June 30, 2006

Differential Expression and Localization of Early Light-Induced Proteins in Arabidopsis thaliana

Mounia Heddad , Hanna Norén , Verena Reiser , Marina Dunaeva , Bertil Andersson , and Iwona Adamska *

Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; Department of Molecular Biology, University of Geneva, 1211 Geneva 4, Switzerland
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; Bio-Rad Laboratories AB, SE-17222 Sundbyberg, Sweden
Department of Physiology and Plant Biochemistry, University of Konstanz, DE-78457 Konstanz, Germany
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; Department of Cardiology, University of Maastricht-Cardiovascular Research Institute of Maastricht, Maastricht, The Netherlands
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; Division of Cell Biology, Linköping University, S-58185 Linköping, Sweden; European Science Foundation, F-67080 Strasbourg-Cedex, France
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; Department of Physiology and Plant Biochemistry, University of Konstanz, DE-78457 Konstanz, Germany

* Corresponding author; email: Iwona.Adamska{at}uni-konstanz.de.

The early light-induced proteins (Elips) in higher plants are nuclear-encoded, light stress-induced proteins located in thylakoid membranes and related to light-harvesting chlorophyll a/b-binding (LHC) proteins. A photoprotective function was proposed for Elips. Here we showed that after 2 h exposure of Arabidopsis (Arabidopsis thaliana) leaves to light stress Elip1 and Elip2 co-isolate equally with monomeric (mLhcb) and trimeric (tLhcb) populations of the major LHC from photosystem II (PSII) as based on the Elip:Lhcb protein ratio. A longer exposure to light stress resulted in increased amounts of Elips in tLhcb as compared to mLhcb, due to a reduction of tLhcb amounts. We demonstrated further that the expression of Elip1 and Elip2 transcripts was differentially regulated in green leaves exposed to light stress. The accumulation of Elip1 transcripts and proteins increased almost linearly with increasing light intensities and correlated with the degree of photoinactivation and photodamage of PSII reaction centers. A stepwise accumulation of Elip2 was induced when 40% of PSII reaction centers became photodamaged. The differential expression of Elip1 and Elip2 occurred also in light stress-preadapted or senescent leaves exposed to light stress but there was a lack of correlation between transcript and protein accumulation. Also in this system the accumulation of Elip1 but not Elip2 correlated with the degree of PSII photodamage. Based on pigment analysis, measurements of PSII activity and assays of the oxidation status of proteins we propose that the discrepancy between amounts of Elip transcripts and proteins in light stress-preadapted or senescent leaves is related to a presence of photoprotective anthocyanins or to lower chlorophyll availability, respectively.




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